Ra. Broglia et G. Tiana, Reading the three-dimensional structure of lattice model-designed proteinsfrom their amino acid sequence, PROTEINS, 45(4), 2001, pp. 421-427
While all the information required for the folding of a protein is containe
d in its amino acid sequence, one has not yet learned how to extract this i
nformation to predict the detailed, biological active, three-dimensional st
ructure of a protein whose sequence is known. Using insight obtained from l
attice model simulations of the folding of small proteins (fewer than 100 r
esidues), in particular of the fact that this phenomenon is essentially con
trolled by conserved contacts (Mirny et al., Proc Natl Acad Sci USA 1995;92
:1282) among (few) strongly interacting ("hot") amino acids (Tiana et al.,
J Chem Phys 1998;108:757-761), which also stabilize local elementary struct
ures formed early in the folding process and leading to the (postcritical)
folding core when they assemble together (Broglia et al., Proc Natl Acad Sc
i USA 1998;95:12930, Broglia & Tiana, J Chem Phys 2001;114:7267), we have w
orked out a successful strategy for reading the three-dimensional structure
of lattice model-designed proteins from the knowledge of only their amino
acid sequence and of the contact energies among the amino acids. (C) 2001 W
iley-Liss, Inc.